Evidence map›Paper›PMID 38247764›Full record

ArticleGels (Basel, Switzerland)2024

Interfacial Rheological Study of β-Casein/Pectin Mixtures at the Air/Water Interface.

Olga Mileti, Noemi Baldino, Stefania Luzzi, Francesca R Lupi, Domenico Gabriele

Open access · goldAbstract read
In one paragraph

Article in Gels (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
2.4field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Olga MiletiDepartment of Information, Modeling, Electronics and System Engineering, (D.I.M.E.S.) University of Calabria, I-87036 Rende, Italy.
Noemi BaldinoDepartment of Information, Modeling, Electronics and System Engineering, (D.I.M.E.S.) University of Calabria, I-87036 Rende, Italy.ORCID 0000-0002-0064-5103
Stefania LuzziDepartment of Information, Modeling, Electronics and System Engineering, (D.I.M.E.S.) University of Calabria, I-87036 Rende, Italy.
Francesca R LupiDepartment of Information, Modeling, Electronics and System Engineering, (D.I.M.E.S.) University of Calabria, I-87036 Rende, Italy.ORCID 0000-0002-1776-0271
Domenico GabrieleDepartment of Information, Modeling, Electronics and System Engineering, (D.I.M.E.S.) University of Calabria, I-87036 Rende, Italy.ORCID 0000-0001-6962-5648
University of Calabria · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Colloidal food products, such as emulsions, foams, gels, and dispersions, are complex systems that need the presence of stabilizing agents to enable their formation and provide stability. Proteins are often used for food foams and emulsions because of their ability to lower interfacial tension and make viscoelastic interfaces. Generally, to improve the resistance against rupture, polysaccharides are used in association with the proteins. Pectin is a complex polysaccharide that can help to stabilize foams or emulsions. This work aims at studying the mechanical resistance of the interface formed by mixtures of β-casein and pectin at high and low methoxylation degrees at the air/water interface using dilatational and shear kinematics. Frequency sweep tests, in the linear region, were performed in shear at different aging times and in dilatational mode, and the rheological data were analyzed. The transient data of the surface tension were analyzed by kinetic models to obtain the characteristic rates of the interfacial phenomena. The kinetic mechanisms of the protein/pectin mixed systems are controlled by protein and show a weak gel behavior for short aging times. The interfaces obtained with both pectins in a mixture with β-casein evolved with time, gelling and showing a solid-like behavior at concentrations of 1 and 10 g/L and after 3.5 h of aging time. The interfacial shear trend obtained suggests a good stabilizing effect of the pectins from citrus with long aging times.

Indexed as

biopolymersmilk proteinsurface tension

Identifiers

PMID38247764
PMCPMC10815610
OpenAlexW4390546740

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.